The basic principle for the synthesis of kestoses involves the action of invertase on sucrose. Invertase hydrolyses sucrose, producing glucose and fructose. Invertase also plays a very important role in kestose synthesis: It transfers the fructosyl residue (resulting from hydrolysis of sucrose) onto the fructose residue of sucrose (1- and 6- kestose) or the glucose residue of sucrose (neo-kestose). In this way, the respective kestoses (1, 6 and neo) are created. The method used for the synthesis of the kestoses was adapted from Gross (1962). 3.2.1. Reagents and instrumentation These kestoses were investigated together because they are synthesised together during the reaction. The following reagents and instruments were used for all optimisation methods …show more content…
All standards, samples and solvents were filtered using filtered using 0.45 µm Sartorius Stedim, cellulose nitrate filter paper prior to HPLC-PAD analysis. The HPLC-PAD system consisted of a PAD detector, Perkin Elmer pump and ALS, CarbopakPA1 (4 × 250 mm) and CarbopakPA1 Guard Column (21.7 °C). The PAD detection range was set at 300 K (E1: 0.05 V, E2: 0.76 V, E3: -0.20 V). The injection volume used for analysis was 50 µL and the analysis time for each sample and standard was set at 30 minutes. The solvent system used for analysis was 10 mM NaOAc/ 150 mM NaOH and the kestoses were eluted at a flow rate of 1 mL /min. 3.2.2. Investigation of reaction parameters There are certain reaction conditions that may favour the production of one kestose isomer over the other. Therefore, several parameters (pH, temperature and time) were chosen and investigated to develop the optimum reaction conditions for each of the kestoses. The experiments for each parameter was carried out in triplicate. Reaction
Catalase Activity on Substrate Based On Gas Pressure Production Rate Name of the Class Author’s Name Date Enzymes are organic compounds which act as catalysts and speed up biological reactions in biological organisms. They are not destroyed or changed during the reaction but rather they are used over and over again to catalyze many more reactions. Their activity may be affected and altered by factors such as temperature, substrate concentration, enzyme concentration and Ph.
Dalia El-Desoky Organic Chemistry II Lab 05 8 February 2017 Dehydration of 2-methylcyclohexanol Introduction: Dehydration is a common reaction in Organic Chemistry used to produce carbon-carbon double bonds. The dehydration mechanism involves the removal of water from an alcohol to form an alkene. In this experiment, 2-methylcyclohexanol will undergo acid catalyzed dehydration in heat to form three products: 1-methylcyclohexene, 3-methylcyclohexene, and methylenecyclohexane [1]. The reaction is carried out in a Hickman still filled with Drierite, a drying agent composed of CaSO4 which absorbs water.
It was expected that an extreme temperature would decrease the rate of reaction and results observed support that idea. With reference to figure 1, the peak performance of catalase was at 30℃, which was the closest to its usual environment
In this laboratory experiment, 3.030 g of Isopentyl Acetate was synthesized and formed by the esterification of acetic acid with Isopentyl Alcohol. 1.0 mL of Sulfuric acid was used as a catalyst in the reaction. The excess Isopentyl Acetate was used to shift the reaction to the right for esterification to occur. During the extraction, the excess of acetic acid and Isopentyl alcohol was extracted with sodium bicarbonate, and further purification of the Isopentyl acetate was done after through drying with anhydrous sodium sulfate and through simple distillation. The percent yield of the Isopentyl Acetate was 46.6 percent with a theoretical yield of 6.502g. In this laboratory experiment the acetic acid was in excess and the Isopentyl Alcohol was the limiting reagent,
Lab Report 5: Acetylsalicylic Acid (Aspirin) Synthesis Name: Divya Mehta Student #: 139006548 Date Conducted: November 19th 2014 Date Submitted: November 26th 2014 Partner’s Name: Kirsten Matthews Lab Section: Wednesday 2:30 L9 IAs Name: Brittany Doerr Procedure: For the procedure, see lab manual (CH110 Lab Manual, Fall 2014) pages 96-98. Wilfrid Laurier University Chemistry Department. Fall 2014. Acetylsalicylic Acid (Aspirin) Synthesis.
Discussion: 1. The Diels alder reaction has to be heated slowly to 60-70 degrees Celsius because if it is heated too quickly and the temperature gets too high the 2,3-dimethyl-1,3-butadiene will boil. A round bottom flask was attached to a water condenser to prevent any product from boiling and evaporating out during the heating process. For the hydrolysis part of the experiment the temperature needed to be 60-80 degrees Celsius to melt the cyclic anhydride but also prevent the reaction from boiling and losing product from evaporation. Lastly the final product crystals were not washed with hot water because it would have melted the crystal thus cold water was used.
Sucrase activity increases with increasing sucrose concentration Materials and Methods Effect of pH on Enzyme Activity 1. Dependent Variable amount of product (glucose and fructose) produced 2. Independent Variable pH 3. Controlled Variables temperature, amount of substrate (sucrose) present, sucrase + sucrose incubation time Effect of Temperature on Enzyme Activity 1.
The objective of this experiment was to use an aldol condensation reaction to synthesize 3-nitrochalcone from 3- nitrobenzaldehyde. This was accomplished with a Diels-Alder reaction that utilized 3-nitrobenzaldehyde, acetophenone, ethanol, and sodium hydroxide. The mechanism for the synthesis of 3-nitrochalcone is presented in Figures 1 and 2. The alpha carbon on the acetophenone is deprotonated. This is followed by the attack of the alpha carbon anion on the carbonyl carbon on the 3-nitrobenzaldehyde.
55 degrees celcius Table 6: Effect of Sucrose Concentration on Sucrase Activity Optical Density 35 g/L 30 g/L 25 g/L 20 g/L 15 g/L 10 g/L 5 g/L 0 g/L 1 1.007 0.974 0.950 0.926 0.849 0.734 0.515 0.003 2 1.002 1.011 0.947 0.937 0.834 0.766 0.496 0.002 3 0.980 0.998 0.944 0.932 0.838 0.754 0.495 0.001 average 0.996 0.994 0.947 0.932 0.840 0.751 0.502 0.002 Effect of Sucrose Concentration on Sucrase Activity 5. State how sucrase activity changes with increasing sucrose concentration. First sucrase activity increases greatly. After 10 g/l sucrase activity continues to increase but at a slow rate until it reaches 30 g/l. At 30 g/l to 35 g/l sucrase activities mostly stayed the same
All electrochemical measurements were performed with an Autolab potentiostat/galvanostat (PGSTAT 101, Eco Chemie, The Netherlands) interfaced with a Nova 1.11 software. A three-electrode system was used in this work consisting of a platinum wire as the auxiliary electrode, an Ag/AgCl/KCl (saturated) as the reference electrode, and a modified carbon paste electrode as the working electrode. A metrohm 827 pH lab (Herisau, Switzerland) supplied with a combination glass-reference electrode was used for pH measurements. 2.2. Materials Acetaminophen powder and TiO2 nanoparticles were purchased from Sigma-Aldrich (Taufkirchen, Germany).
TLC was used to identify the actual unknown product as well as other products/reactants present in the filtered solution. The procedure was conducted by placing a TLC plate in a developing chamber that is filled with a small amount of solvent. The solvent cannot be too polar because it will cause spotted compounds on the TLC plate to rise up too fast, while a very non-polar solvent will not allow the spots to move. The polarity of the spots also determines how far it moves on the plate; non-polar spots are higher than polar ones. After spots on the TLC form, the Rf values are calculated and used to analyze the similarity of the compounds.
Enzymes speed up chemical reactions enabling more products to be formed within a shorter span of time. Enzymes are fragile and easily disrupted by heat or other mild treatment. Studying the effect of temperature and substrate concentration on enzyme concentration allows better understanding of optimum conditions which enzymes can function. An example of an enzyme catalyzed reaction is enzymatic hydrolysis of an artificial substrate, o-Nitrophenylgalactoside (ONPG) used in place of lactose. Upon hydrolysis by B-galactosidase, a yellow colored compound o-Nitrophenol (ONP) is formed.
This verified the formation of the major products. Overall, one can say that the experiment was
Introduction 1.1 Aim: To determine the kinetic parameters, Vmax and Km, of the alkaline phosphatase enzyme through the determination of the optimum pH and temperature. 1.2 Theory and Principles (General Background): Enzymes are highly specific protein catalysts that are utilised in chemical reactions in biological systems.1 Enzymes, being catalysts, decrease the activation energy required to convert substrates to products. They do this by attaching to the substrate to form an intermediate; the substrate binds to the active site of the enzyme. Then, another or the same enzyme reacts with the intermediate to form the final product.2 The rate of enzyme-catalysed reactions is influenced by different environmental conditions, such as: concentration
By observing figure 3, the more enzyme that is available, the faster the reaction rate is. The optimal enzyme concentration was chosen based on the R2 values from figure 2. The highest observable rate also had the best R2 number, which was closest to one. This enzyme concentration was used in part 2.